BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5δ

Xu, Lixin; Yang, Lihong; Moitra, Prasun; Hashimoto, Keiko; Rallabhandi, Prasad; Kaul, Sunil C.; Meroni, Germana; Jensen, Jane P.; Weissman, Allan M.; D’Arpa, Peter

doi:10.1016/s0014-4827(03)00187-3

Cited by 98 publications

(77 citation statements)

References 47 publications

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“…Furthermore, a splice variant from the TRIM5 gene, TRIM5␦, can direct autoubiquitylation (20). The RING domain is required for efficient restriction by rhTRIM5␣ (33,34), yet we show here, consistent with others, that disrupting proteasome function does not relieve rhTRIM5␣-mediated restriction of HIV-1 infection (29).…”

Section: Discussionsupporting

confidence: 86%

“…TRIM family members form high-order molecular-weight structures via their coiled coil regions, generating intracellular structures or bodies (19). The RING domain also has E3 ubiquitin ligase activity in some TRIM members like human TRIM5␦ (20), fostering speculation that TRIM5␣ restriction may also involve proteasome activity (16). Many TRIM proteins also contain a carboxy-terminal motif specific for the TRIM family member.…”

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confidence: 99%

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Proteasome inhibitors uncouple rhesus TRIM5α restriction of HIV-1 reverse transcription and infection

Anderson

Campbell

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

246

292

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Section: Discussionsupporting

confidence: 86%

mentioning

confidence: 99%

Proteasome inhibitors uncouple rhesus TRIM5α restriction of HIV-1 reverse transcription and infection

Anderson

Campbell

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

246

292

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“…TRIM5␣ is a postentry restriction factor that accounts for the resistance to HIV type 1 (HIV-1) observed in rhesus monkey cells. It is not yet known how TRIM5␣ mediates viral restriction, although a shorter, alternate transcript of the TRIM5 gene has been shown to be an ubiquitin ligase (5). TRIM5␣ restriction depends on the viral capsid, and its effect is saturable (4), although direct physical interaction between TRIM5␣ and capsid has not been demonstrated.…”

mentioning

confidence: 99%

Positive selection of primate TRIM5 α identifies a critical species-specific retroviral restriction domain

Sawyer

Emerman

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

646

677

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Primate genomes encode a variety of innate immune strategies to defend themselves against retroviruses. One of these, TRIM5␣, can restrict diverse retroviruses in a species-specific manner. Thus, whereas rhesus TRIM5␣ can strongly restrict HIV-1, human TRIM5␣ only has weak HIV-1 restriction. The biology of TRIM5␣ restriction suggests that it is locked in an antagonistic conflict with the proteins encoding the viral capsid. Such antagonistic interactions frequently result in rapid amino acid replacements at the proteinprotein interface, as each genetic entity vies for evolutionary dominance. By analyzing its evolutionary history, we find strong evidence for ancient positive selection in the primate TRIM5␣ gene. This selection is strikingly variable with some of the strongest selection occurring in the human lineage. This history suggests that TRIM5␣ evolution has been driven by antagonistic interactions with a wide variety of viruses and endogenous retroviruses that predate the origin of primate lentiviruses. A 13-aa ''patch'' in the SPRY protein domain bears a dense concentration of positively selected residues, potentially implicating it as an antiviral interface. By using functional studies of chimeric TRIM5␣ genes, we show that this patch is generally essential for retroviral restriction and is responsible for most of the species-specific antiretroviral restriction activity. Our study highlights the power of evolutionary analyses, in which positive selection identifies not only the age of genetic conflict but also the interaction interface where this conflict plays out.capsid ͉ human endogenous retroviruses ͉ HIV type 1 ͉ SPRY

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“…First, the BTBD1 sequence is highly similar to the BTBD2 sequence, which has been shown in vitro to slightly inhibit Topo1 activity on DNA. Moreover, Xu et al 40 recently described the cellular colocalization of BTBD1 and BTBD2 to cytoplasmic bodies with TRIM5d, which is a member of the TRIM protein family. Interestingly, these proteins have ubiquitin ligase and multimerization activities.…”

Section: Does Btbd1 Function As a General Topo1 Degradation Regulator?mentioning

confidence: 99%

“…21,26 At this point, it is not clear whether the Topo1-BTBD1 interactions take place in the nucleus or in the cytoplasm. Since BTBD1 has been localized in cytoplasmic bodies, 40 the simplest hypothesis to explain BTBD1 function is that BTBD1 binds to Topo1 through its C-terminal BTB domain after Topo1 transportation in the cytoplasm. The N-terminal BTB domain would interact with the appropriate proteins to address Topo1 to proteasome.…”

Section: Does Btbd1 Function As a General Topo1 Degradation Regulator?mentioning

confidence: 99%

The topoisomerase 1-interacting protein BTBD1 is essential for muscle cell differentiation

et al. 2004

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DNA topoisomerase I (Topo1) contributes to vital biological functions, but its regulation is not clearly understood. The BTBD1 protein was recently cloned on the basis of its interaction with the core domain of Topo1 and is expressed particularly in skeletal muscle. To determine BTBD1 functions in this tissue, the in vitro model used was the C2C12 mouse muscle cell line, which expresses BTBD1 mainly after myotube differentiation. We studied the effects of a stably overexpressed BTBD1 protein truncated of the 108 N-terminal amino-acid residues and harbouring a C-terminal FLAG tag (D-BTBD1). The proliferation speed of D-BTBD1 C2C12 cells was significantly decreased and no myogenic differentiation was observed, although these cells maintained their capacity to enter adipocyte differentiation. These alterations could be related to Topo1 deregulation. This hypothesis is further supported by the decrease in nuclear Topo1 content in D-BTBTD1 proliferative C2C12 cells and the switch from the main peripheral nuclear localization of Topo1 to a mainly nuclear diffuse localization in D-BTBTD1 C2C12 cells. Finally, this study demonstrated that BTBD1 is essential for myogenic differentiation.

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BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5δ

Cited by 98 publications

References 47 publications

Proteasome inhibitors uncouple rhesus TRIM5α restriction of HIV-1 reverse transcription and infection

Proteasome inhibitors uncouple rhesus TRIM5α restriction of HIV-1 reverse transcription and infection

Positive selection of primate TRIM5 α identifies a critical species-specific retroviral restriction domain

The topoisomerase 1-interacting protein BTBD1 is essential for muscle cell differentiation

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